Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

System specificity of the TpsB transporters of coexpressed two-partner secretion systems of Neisseria meningitidis.

Journal of bacteriology - 1 Feb 2013

ur Rahman Sadeeq, van Ulsen Peter

Abstract excerpt

The two-partner secretion (TPS) systems of Gram-negative bacteria consist of a large secreted exoprotein (TpsA) and a transporter protein (TpsB) located in the outer membrane. TpsA targets TpsB for transport across the membrane via its ∼30-kDa TPS domain located at its N terminus, and this domain is also the minimal secretory unit. Neisseria meningitidis genomes encode up to five TpsAs and two TpsBs. Sequence...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacterial Outer Membrane Proteins
Share to Carrier Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Computer Simulation

Share to Gene Deletion

Share to Gene Expression Regulation, Bacterial

Share to Neisseria meningitidis

Share to Protein Conformation

Share to Species Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 23222722
DOI: 10.1128/JB.01355-12
PMCID: PMC3562106

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

System specificity of the TpsB transporters of coexpressed two-partner secretion systems of Neisseria meningitidis.PMID 23222722Read ↗

A Functional Two-Partner Secretion System Contributes to Adhesion of <i>Neisseria meningitidis</i> to Epithelial CellsSemantic proximity Read ↗

Biological Functions of the Secretome of Neisseria meningitidisSemantic proximity Read ↗

ESX/Type VII Secretion Systems—An Important Way Out for Mycobacterial ProteinsSemantic proximity Read ↗

Large‐scale study of the interactions between proteins involved in type IV pilus biology in Neisseria meningitidis : characterization of a subcomplex involved in pilus assemblySemantic proximity Read ↗

Type V Protein Secretion Pathway: the Autotransporter StorySemantic proximity Read ↗

Type V Secretion Systems in Bacteria.Semantic proximity Read ↗

Modification of a PE/PPE substrate pair reroutes an Esx substrate pair from the mycobacterial ESX-1 type VII secretion system to the ESX-5 systemSemantic proximity Read ↗

Identification of a novel two-partner secretion system from Burkholderia pseudomallei.Semantic proximity Read ↗

PPE and PE_PGRS proteins of <i>Mycobacterium marinum</i> are transported via the type VII secretion system ESX‐5Semantic proximity Read ↗

Secretion signal of the filamentous haemagglutinin, a model two-partner secretion substrate.Semantic proximity Read ↗

Molecular characteristics of the CupB chaperone-usher pathway and the Tps4 two-partner secretion system in Pseudomonas aeruginosaSemantic proximity Read ↗

Insights into the complex formation of a trimeric autotransporter adhesin with a peptidoglycan-binding periplasmic proteinSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.